| IED ID | IndEnz0002014215 |
| Enzyme Type ID | protease014215 |
| Protein Name |
Aminopeptidase Ey EC 3.4.11.20 Aminopeptidase N |
| Gene Name | ANPEP APDE |
| Organism | Gallus gallus (Chicken) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Sauropsida Sauria (diapsids) Archelosauria Archosauria Dinosauria Saurischia Theropoda Coelurosauria Aves Neognathae Galloanserae Galliformes Phasianidae (turkeys) Phasianinae Gallus Gallus gallus (Chicken) |
| Enzyme Sequence | MAAGFFISKSVGIVGIVLALGAVATIIALSVVYAQEKNKSSGGSGGSDTTSTTTASTTTTSTTTASTTAAPNNPWNRWRLPTALKPESYEVTLQPFLTPDDNNMYIFKGNSSVVFLCEEATDLILIHSNKLNYTLQGGFHASLHAVNGSTPPTISNTWLETNTQYLVLQLAGPLQQGQHYRLFSIFTGELADDLAGFYRSEYTEGNVTKVVATTQMQAPDARKAFPCFDEPAMKAVFTVTMIHPSDHTAISNMPVHSTYQLQMDGQSWNVTQFDPTPRMSTYLLAFIVSQFDYVENNTGKVQIRIWGRPAAIAEGQGEYALEKTGPILSFFERHYNTAYPLPKSDQVGLPDFNAGAMENWGLVTYRENSLLYDNAYSSIGNKERVVTVIAHELAHQWFGNLVTLRWWNDLWLNEGFASYVEYLGADSAEPTWDIKDLMVLNELYTVMATDALTTSHPLTFREDEINTPAQISEVFDSIAYSKGASVLRMLSDFLTEDVFKEGLQSYLHDFSYNNTVYTDLWDHLQEAVNKNSVPLPDSIGAIMDRWTLQMGFPVVTVNTLTGSVQQSHFLLDSNSTVERPSVFNYTWIVPITWMTPSRTGDRYWLVDVSATNSDFSVGSSTWLLLNLNVSGYFRVNYNQENWDQLLQQLSNNHQAIPVINRAQIIDDAFNLARAQQVSVTLALNTTRFLSGETAYMPWQAALNNLQYFQLMFDRSEVFGAMTKYIQKQVTPLFEYYRTATNNWTAIPSALMDQYNEINAISTACSYGIAECQQLATALYQQWRQNVSNNPIAPNLRSAIYCSAVATGGEEVWDFIWERFLEAPVVSEADKLRTALTCSTETWILQRYLQYTIDPTKIRKQDATSTINSIASNVVGQPLAWDFIRSNWRTLFGQYGGGSFSFSRLISAVTQRFNTEFELKQLEQFKADNQDIGFGSGTRALEQALERTRTNINWVKENKEVVHAWFRAETASS |
| Enzyme Length | 972 |
| Uniprot Accession Number | O57579 |
| Absorption | |
| Active Site | ACT_SITE 392; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Differs from other aminopeptidases in broad specificity for amino acids in the P1 position and the ability to hydrolyze peptides of four or five residues that contain Pro in the P1' position.; EC=3.4.11.20; Evidence={ECO:0000269|PubMed:7684960, ECO:0000269|PubMed:8205380}; |
| DNA Binding | |
| EC Number | 3.4.11.20 |
| Enzyme Function | FUNCTION: Broad specificity aminopeptidase. Degrades a variety of peptides possessing various N-terminal amino acids including hydrophobic, basic and acidic amino acids. Preferentially hydrolyzes small peptides consisting of 4 or 5 amino acids. Hydrolyzes the N-terminal Xaa-Pro bonds in the chicken brain peptide Leu-Pro-Leu-Arg-PheNH2, the substance P fragment Arg-Pro-Lys-Pro and the bradykinin fragment Arg-Pro-Pro-Gly-Phe. Hydrolyzes the N-formylated peptides fMet-Leu-Phe, fMet-Ala-Gly-Ser-Glu and fMet-Nle-Leu-Phe-Nle-Tyr-Lys, but does not hydrolyze peptides with acetylation or pyroglutamic acid at N-terminus. Does not hydrolyze large peptides such as complete substance P, bradykinin or schistoFLRFamide. {ECO:0000269|PubMed:7684960, ECO:0000269|PubMed:8205380, ECO:0000269|Ref.4}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Compositional bias (1); Disulfide bond (2); Glycosylation (14); Initiator methionine (1); Metal binding (3); Region (4); Sequence conflict (9); Site (1); Topological domain (2); Transmembrane (1) |
| Keywords | Aminopeptidase;Cell membrane;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Signal-anchor;Transmembrane;Transmembrane helix;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|Ref.4}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P15144}. Note=Also found as a soluble form. {ECO:0000269|Ref.4}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 109,132 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.58 mM for Leu-Pro-Leu-Arg-PheNH2 {ECO:0000269|PubMed:7684960, ECO:0000269|PubMed:8205380}; KM=1.23 mM for fMet-Leu-Phe {ECO:0000269|PubMed:7684960, ECO:0000269|PubMed:8205380}; KM=1.53 mM for fMet-Ala-Gly-Ser-Glu {ECO:0000269|PubMed:7684960, ECO:0000269|PubMed:8205380}; KM=1.72 mM for fMet-Nle-Leu-Phe-Nle-Tyr-Lys {ECO:0000269|PubMed:7684960, ECO:0000269|PubMed:8205380}; |
| Metal Binding | METAL 391; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 395; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 414; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.11.20; |